PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24751575-6	2014	We screened 542 chemicals for the inhibition potency toward hydrolase activities of p-nitrophenyl acetate by recombinant CES1, CES2, and AADAC.	4-nitrophenyl acetate	84-105	carboxylesterase 1	Homo sapiens	121-125	
34142538-3	2021	In this work, the molecular mechanism of the hydrolysis reaction of para-nitrophenyl acetate in the active site of human carboxylesterase was determined using modern methods of molecular modeling.	4-nitrophenyl acetate	68-92	carboxylesterase 1	Homo sapiens	121-137	
24141856-8	2014	Additionally, we screened a panel of therapeutic drugs and drugs of abuse to assess their inhibition of the hydrolysis of p-nitrophenyl acetate by recombinant CES1 and human liver microsomes.	4-nitrophenyl acetate	122-143	carboxylesterase 1	Homo sapiens	159-163	
20097249-6	2010	In vitro studies were performed using previously developed cell lines which overexpress hCES1 with both p-nitrophenyl acetate and d-MPH serving as known substrates.	4-nitrophenyl acetate	104-125	carboxylesterase 1	Homo sapiens	88-93	
21540359-4	2011	With 4-nitrophenyl acetate (4-NPA) as the probe substrate, the K(m) values of recombinant CES1-b and CES2 matched those of human liver microsomes (HLM) and human intestinal microsomes (HIM) with approximately 200 and 180 muM, respectively.	4-nitrophenyl acetate	5-26	carboxylesterase 1	Homo sapiens	90-94